| IED ID | IndEnz0001000418 |
| Enzyme Type ID | amylase000418 |
| Protein Name |
Alpha-amylase 1 EC 3.2.1.1 1,4-alpha-D-glucan glucanohydrolase 1 |
| Gene Name | AMY1 |
| Organism | Schwanniomyces occidentalis (Yeast) (Debaryomyces occidentalis) |
| Taxonomic Lineage | cellular organisms Eukaryota Opisthokonta Fungi Dikarya Ascomycota saccharomyceta Saccharomycotina (true yeasts) Saccharomycetes Saccharomycetales Debaryomycetaceae Schwanniomyces Schwanniomyces occidentalis (Yeast) (Debaryomyces occidentalis) |
| Enzyme Sequence | MRFSTEGFTSKVVAAILAFSRLVSAQPIIFDMRDVSSSADKWKDQSIYQIVTDRFARSDGSTTADCLVSDRKYCGGSYKGIIDKLDYIQGMGFTAIWISPVVEQIPDNTAYGYAYHGYWMKNIDELNTNFGTADELKQLASELHSRSMLLMVDVVYNHYAWNGDGSSVDYSSFTPFNQQSYFHDYCLITNYNDQTNVEDCWEGDTEVSLPDLSTEDNEVIGVFQTWVSDFVQNYSIDGLRIDSAKHVDTASLTKFEDASGVYNLGEVYQGDPTYTCPYQNYMKGVTNYPLYYPVYRFFSDTSATSSELTSMISTLQSSCSDVSLLGNFIENHDQVRFPSVTSDTSLIKNDMAFIILGDGIPIIYYGQEQGLNGGSDPANREALWLSGYNTDSEYYELISKLNQIRNQAIKKDSAYSTYKSSVVSSSDHYIATRKGSDANQLISIFNNLGSNGSQDITVSNTGYSSGDKVIDIISCNSVLAGDSGSLSVSISGGMPQVYAPSSVLSGSGICNQ |
| Enzyme Length | 512 |
| Uniprot Accession Number | P19269 |
| Absorption | |
| Active Site | ACT_SITE 242; /note=Nucleophile; /evidence=ECO:0000250|UniProtKB:P56271; ACT_SITE 266; /note=Proton donor; /evidence=ECO:0000250|UniProtKB:P56271 |
| Activity Regulation | ACTIVITY REGULATION: Alpha-amylase expression underlies catabolite repression by glucose. |
| Binding Site | BINDING 119; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P0C1B3; BINDING 158; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P0C1B3; BINDING 240; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P0C1B3; BINDING 270; /note=Substrate; via amide nitrogen; /evidence=ECO:0000250|UniProtKB:P0C1B3; BINDING 333; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P0C1B3; BINDING 380; /note=Substrate; /evidence=ECO:0000250|UniProtKB:P0C1B3 |
| Calcium Binding | |
| catalytic Activity | CATALYTIC ACTIVITY: Reaction=Endohydrolysis of (1->4)-alpha-D-glucosidic linkages in polysaccharides containing three or more (1->4)-alpha-linked D-glucose units.; EC=3.2.1.1; Evidence={ECO:0000269|PubMed:2806251}; |
| DNA Binding | |
| EC Number | 3.2.1.1 |
| Enzyme Function | |
| Temperature Dependency | |
| PH Dependency | |
| Pathway | |
| nucleotide Binding | |
| Features | Active site (2); Binding site (6); Chain (1); Disulfide bond (4); Glycosylation (1); Metal binding (6); Natural variant (7); Region (1); Signal peptide (1); Site (1) |
| Keywords | Calcium;Carbohydrate metabolism;Disulfide bond;Glycoprotein;Glycosidase;Hydrolase;Metal-binding;Secreted;Signal |
| Interact With | |
| Induction | |
| Subcellular Location | SUBCELLULAR LOCATION: Secreted {ECO:0000269|PubMed:2806251}. |
| Modified Residue | |
| Post Translational Modification | |
| Signal Peptide | SIGNAL 1..25; /evidence=ECO:0000255 |
| Structure 3D | |
| Cross Reference PDB | - |
| Mapped Pubmed ID | - |
| Motif | |
| Gene Encoded By | |
| Mass | 56,527 |
| Kinetics | |
| Metal Binding | METAL 157; /note=Calcium 1; /evidence=ECO:0000250|UniProtKB:P0C1B3; METAL 198; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P56271; METAL 211; /note=Calcium 1; /evidence=ECO:0000250|UniProtKB:P56271; METAL 242; /note=Calcium 2; /evidence=ECO:0000250|UniProtKB:P0C1B3; METAL 246; /note=Calcium 1; via carbonyl oxygen; /evidence=ECO:0000250|UniProtKB:P0C1B3; METAL 266; /note=Calcium 2; /evidence=ECO:0000250|UniProtKB:P0C1B3 |
| Rhea ID | |
| Cross Reference Brenda |